RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins.
about
Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-IDual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processingStructures of Cryptococcus neoformans Protein Farnesyltransferase Reveal Strategies for Developing Inhibitors That Target Fungal PathogensPurified yeast protein farnesyltransferase is structurally and functionally similar to its mammalian counterpart.Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavageThe multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor.Identification of yeast component A: reconstitution of the geranylgeranyltransferase that modifies Ypt1p and Sec4p.Chemical inhibition of CaaX protease activity disrupts yeast Ras localization.Mutations in the SHR5 gene of Saccharomyces cerevisiae suppress Ras function and block membrane attachment and palmitoylation of Ras proteins.Molecular basis of cell integrity and morphogenesis in Saccharomyces cerevisiaeThe Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Ste14p is in the endoplasmic reticulum membrane.Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity.SET1, a yeast member of the trithorax family, functions in transcriptional silencing and diverse cellular processes.Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytesA novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursorTowards the systematic mapping and engineering of the protein prenylation machinery in Saccharomyces cerevisiaeCloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferaseMultiple domain insertions and losses in the evolution of the Rab prenylation complex.Enlarged meristems and delayed growth in plp mutants result from lack of CaaX prenyltransferases.The role of lipid post-translational modification in plant developmental processesComplex fate of paralogs.Metabolic Adaptation to Nutrients Involves Coregulation of Gene Expression by the RNA Helicase Dbp2 and the Cyc8 Corepressor in Saccharomyces cerevisiae.Genome-wide gene expression profiling of fertilization competent mycelium in opposite mating types in the heterothallic fungus Podospora anserina.Dual lipid modification of the yeast ggamma subunit Ste18p determines membrane localization of Gbetagamma.Site-directed mutations altering the CAAX box of Ste18, the yeast pheromone-response pathway G gamma subunit.On the physiological importance of endoproteolysis of CAAX proteins: heart-specific RCE1 knockout mice develop a lethal cardiomyopathy.Yeast glucose pathways converge on the transcriptional regulation of trehalose biosynthesis.Prelamin A, Zmpste24, misshapen cell nuclei, and progeria--new evidence suggesting that protein farnesylation could be important for disease pathogenesis.Protein kinase A regulates constitutive expression of small heat-shock genes in an Msn2/4p-independent and Hsf1p-dependent manner in Saccharomyces cerevisiae.Mutant farnesyltransferase beta subunit of Saccharomyces cerevisiae that can substitute for geranylgeranyltransferase type I beta subunit.Chimeric protein complexes in hybrid species generate novel phenotypesConsequences of altered isoprenylation targets on a-factor export and bioactivity.Self-induction of a/a or alpha/alpha biofilms in Candida albicans is a pheromone-based paracrine system requiring switchingRas signaling in yeast.Roles of Ras1 membrane localization during Candida albicans hyphal growth and farnesol responseSevere hepatocellular disease in mice lacking one or both CaaX prenyltransferases.Identification of Ras farnesyltransferase inhibitors by microbial screening.Biogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease.Biogenesis of the Saccharomyces cerevisiae mating pheromone a-factor.Arabidopsis Rab Geranylgeranyltransferases Demonstrate Redundancy and Broad Substrate Specificity in Vitro
P2860
Q24530008-F8B92D3C-F3F7-4FBE-A2EF-882C323224D4Q24670437-E4331C93-BDE4-407D-A40F-9BA730BE93FBQ27671538-2C9723E3-9A52-4C96-BBEB-05A7980E4589Q27929835-7FBE3A64-35D0-44A9-A20A-F355CCB10551Q27931598-DDCB93E3-3014-42B8-8743-F6E1E978DCF3Q27935263-1C6D5FD6-EF60-4D12-B27D-7453951959F2Q27935697-12BE1C16-0DF4-49E9-847F-C4D5B2B21A5BQ27937343-6901C47D-D82E-4B74-A68A-DACD24261EBEQ27937744-E93A98CB-721A-44AD-B529-7093C84A593BQ27937824-EB0A20F4-18F8-4375-958E-678067DA4468Q27937876-94235EBA-1321-4E4E-B398-AB8793407358Q27939243-67B7BF1E-6A20-405F-8F3E-B92F17F57452Q27939597-1EAAF2BD-EF01-404B-B86C-616667F1F520Q28296170-1B5AE040-0058-4CE9-B5BB-743B3300167BQ28493191-D5A25855-5139-4EDB-958B-3012E233C3EDQ28544006-A1842703-DD50-4209-BB73-1B473BF1220FQ28581840-DCEA2719-7C9A-45B8-B1A9-DE0117DFFBB6Q33294515-D7B96182-F1B9-48C2-9416-2A79663280E0Q33339999-EA092E0F-7F4E-4D57-9E6F-B057749D6485Q33357999-559C78FF-3950-422B-A2E7-C10F579D7F5AQ33394390-7F95DBEB-5989-4A69-8AA3-151D1CA58F3EQ33877348-89379173-806B-4D36-91E3-6000392BFD2EQ33954941-84903EB3-CACD-4273-8DA2-1A00C2C60EE6Q33960304-F371AF82-A5A1-49FA-96F6-D08001FE1DD1Q33963393-5D2224FB-5711-443A-A842-C37D690F3652Q34277651-CE4FC53B-FD95-4287-9D3F-D02C1459770AQ34304001-974D5AB0-FBFC-4776-9874-ADB0AFDB69EDQ34457223-A1002512-CDB9-4770-997B-9EF713DC6DB8Q34572425-AC6B2C00-46DE-46AF-89F5-B54D76E77023Q34649429-4FA68A9A-7043-4BD9-8410-1E5DAF5876B9Q35020218-092E95A0-757C-4DB6-9B27-130329C0A165Q35038534-BCAC3E53-D8BE-434C-80EC-E5828EA49434Q35080875-F55530C6-DFAE-4F60-A727-CD3C5D8806E1Q35083712-2E2C9F2F-C7AF-4904-9B48-378D7F378743Q35530373-23C5D375-B61B-4C71-A032-89B196564708Q35625978-6D256316-B072-4AF8-80CB-A5C82A29D0A0Q36165226-EE8C5C5E-DFB8-430B-94AA-9231E7D72EDEQ36194945-1A775A15-BD04-45B1-8704-56899C11AFFAQ36259400-45DE86AC-3A91-4596-BF24-99DB819F60C9Q36466195-F3329596-418D-4D20-9B5E-AE64DAA931B0
P2860
RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins.
description
1991 nî lūn-bûn
@nan
1991 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
name
RAM2, an essential gene of yea ...... tes a-factor and Ras proteins.
@ast
RAM2, an essential gene of yea ...... tes a-factor and Ras proteins.
@en
RAM2, an essential gene of yea ...... tes a-factor and Ras proteins.
@nl
type
label
RAM2, an essential gene of yea ...... tes a-factor and Ras proteins.
@ast
RAM2, an essential gene of yea ...... tes a-factor and Ras proteins.
@en
RAM2, an essential gene of yea ...... tes a-factor and Ras proteins.
@nl
prefLabel
RAM2, an essential gene of yea ...... tes a-factor and Ras proteins.
@ast
RAM2, an essential gene of yea ...... tes a-factor and Ras proteins.
@en
RAM2, an essential gene of yea ...... tes a-factor and Ras proteins.
@nl
P2860
P3181
P356
P1476
RAM2, an essential gene of yea ...... tes a-factor and Ras proteins.
@en
P2860
P3181
P356
10.1073/PNAS.88.24.11373
P407
P577
1991-12-15T00:00:00Z